Fumarate hydratase class II - Escherichia coli (strain K12)

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Reviewed, UniProtKB/Swiss-Prot P05042 (FUMC_ECOLI)

Last modified June 16, 2009. Version 104. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Fumarate hydratase class II
      Short name=Fumarase C
    EC=4.2.1.2

Gene names

Name:	fumC
Ordered Locus Names:	b1611, JW1603

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	467 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Catalytic activity	(S)-malate = fumarate + H₂O. HAMAP MF_00743
Pathway	Carbohydrate metabolism; tricarboxylic acid cycle. HAMAP MF_00743
Subunit structure	Homotetramer. Ref.11
Subcellular location	Cytoplasm. HAMAP MF_00743
Miscellaneous	There are 2 substrate binding sites: the catalytic A site, and the non-catalytic B site that may play a role in the transfer of substrate or product between the active site and the solvent. Alternatively, the B site may bind allosteric effectors. HAMAP MF_00743
Sequence similarities	Belongs to the class-II fumarase/aspartase family. Fumarase subfamily.

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Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Cellular component	Cytoplasm
Molecular function	Lyase
Technical term	3D-structure Allosteric enzyme Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	fumarate metabolic process Inferred from electronic annotation. Source: InterPro tricarboxylic acid cycle Inferred from electronic annotation. Source: HAMAP
Cellular component	tricarboxylic acid cycle enzyme complex Inferred from electronic annotation. Source: InterPro
Molecular function	fumarate hydratase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 467

467

Fumarate hydratase class II HAMAP MF_00743

PRO_0000161275

Regions

Region

126 – 132

B site HAMAP MF_00743

Region

139 – 141

Substrate binding HAMAP MF_00743

Sites

Binding site

100

Substrate HAMAP MF_00743

Experimental info

Mutagenesis

126

R → A: Reduces enzyme activity 10-fold. Ref.10

Mutagenesis

127

K → D: No effect. Ref.10

Mutagenesis

129

H → N: No effect on activity. Ref.10 Ref.12

Mutagenesis

188

H → N: Reduces activity 200-fold. Ref.12

Mutagenesis

315

E → Q: Reduces activity 10-fold. Ref.13

Secondary structure

467

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P05042-1 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: 3D67E3C0F0FDF40B
Show »

FASTA

467

50,489

        10         20         30         40         50         60 
MNTVRSEKDS MGAIDVPADK LWGAQTQRSL EHFRISTEKM PTSLIHALAL TKRAAAKVNE 

        70         80         90        100        110        120 
DLGLLSEEKA SAIRQAADEV LAGQHDDEFP LAIWQTGSGT QSNMNMNEVL ANRASELLGG 

       130        140        150        160        170        180 
VRGMERKVHP NDDVNKSQSS NDVFPTAMHV AALLALRKQL IPQLKTLTQT LNEKSRAFAD 

       190        200        210        220        230        240 
IVKIGRTHLQ DATPLTLGQE ISGWVAMLEH NLKHIEYSLP HVAELALGGT AVGTGLNTHP 

       250        260        270        280        290        300 
EYARRVADEL AVITCAPFVT APNKFEALAT CDALVQAHGA LKGLAASLMK IANDVRWLAS 

       310        320        330        340        350        360 
GPRCGIGEIS IPENEPGSSI MPGKVNPTQC EALTMLCCQV MGNDVAINMG GASGNFELNV 

       370        380        390        400        410        420 
FRPMVIHNFL QSVRLLADGM ESFNKHCAVG IEPNRERINQ LLNESLMLVT ALNTHIGYDK 

       430        440        450        460 
AAEIAKKAHK EGLTLKAAAL ALGYLSEAEF DSWVRPEQMV GSMKAGR

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structural and functional relationships between fumarase and aspartase. Nucleotide sequences of the fumarase (fumC) and aspartase (aspA) genes of Escherichia coli K12." Woods S.A., Miles J.S., Roberts R.E., Guest J.R. Biochem. J. 237:547-557(1986) [PubMed: 3541901] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. Horiuchi T. DNA Res. 3:363-377(1996) [PubMed: 9097039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Complete nucleotide sequence of the fumarase gene fumA, of Escherichia coli." Miles J.S., Guest J.R. Nucleic Acids Res. 12:3631-3642(1984) [PubMed: 6328431] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-89.
[6]	"The fumarase genes of Escherichia coli: location of the fumB gene and discovery of a new gene (fumC)." Guest J.R., Miles J.S., Roberts R.E., Woods S.A. J. Gen. Microbiol. 131:2971-2984(1985) [PubMed: 3005475] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-89.
[7]	"Purification and characterization of two types of fumarase from Escherichia coli." Ueda Y., Yumoto N., Tokushige M., Fukui K., Ohya-Nishiguchi H. J. Biochem. 109:728-733(1991) [PubMed: 1917897] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-20.
[8]	"Purification and crystallization of fumarase C from Escherichia coli." Weaver T.M., Levitt D.G., Banaszak L.J. J. Mol. Biol. 231:141-144(1993) [PubMed: 8496960] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-15, CHARACTERIZATION.
[9]	"Two biochemically distinct classes of fumarase in Escherichia coli." Woods S.A., Shwartzbach S.D., Guest J.R. Biochim. Biophys. Acta 954:14-26(1988) [PubMed: 3282546] [Abstract] Cited for: BIOCHEMICAL ANALYSIS OF FUMA AND FUMC.
[10]	"The role of the allosteric B site in the fumarase reaction." Rose I.A., Weaver T.M. Proc. Natl. Acad. Sci. U.S.A. 101:3393-3397(2004) [PubMed: 14990798] [Abstract] Cited for: MUTAGENESIS OF ARG-126; LYS-127 AND HIS-129.
[11]	"Crystallographic studies of the catalytic and a second site in fumarase C from Escherichia coli." Weaver T., Banaszak L. Biochemistry 35:13955-13965(1996) [PubMed: 8909293] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS), SUBUNIT.
[12]	"Mutations of fumarase that distinguish between the active site and a nearby dicarboxylic acid binding site." Weaver T., Lees M., Banaszak L. Protein Sci. 6:834-842(1997) [PubMed: 9098893] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF MUTANTS ASN-129 AND ASN-188 IN COMPLEX WITH MALATE AND CITRATE, MUTAGENESIS OF HIS-129 AND HIS-188.
[13]	"X-ray crystallographic and kinetic correlation of a clinically observed human fumarase mutation." Estevez M., Skarda J., Spencer J., Banaszak L., Weaver T.M. Protein Sci. 11:1552-1557(2002) [PubMed: 12021453] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF MUTANT GLN-315, MUTAGENESIS OF GLU-315.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

X04065 Genomic DNA. Translation: CAA27698.1.
U00096 Genomic DNA. Translation: AAC74683.1.
AP009048 Genomic DNA. Translation: BAA15349.1.
X00522 Genomic DNA. Translation: CAA25205.1.

PIR

UFEC. S07138.

RefSeq

AP_002232.1.
NP_416128.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FUO	X-ray	1.98	A/B	1-467	[»]
1FUP	X-ray	2.30	A/B	1-467	[»]
1FUQ	X-ray	2.00	A/B	1-467	[»]
1FUR	X-ray	1.95	A/B	1-467	[»]
1KQ7	X-ray	2.60	A/B	1-467	[»]
1YFE	X-ray	2.19	A	1-467	[»]
2FUS	X-ray	2.20	A/B	1-467	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:9719N.

2-D gel databases

ECO2DBASE

H050.4. 6TH EDITION.

Genome annotation databases

GeneID

946147.

GenomeReviews

Gene locus JW1603 in contig AP009048_GR.
Gene locus b1611 in contig U00096_GR.

KEGG

ecj:JW1603.
eco:b1611.

Organism-specific databases

EchoBASE

EB0353.

EcoGene

EG10358. fumC.

CMR

Search...

Phylogenomic databases

HOGENOM

P05042.

OMA

P05042. GSQGHFE.

Enzyme and pathway databases

BioCyc

EcoCyc:FUMC-MON.
MetaCyc:FUMC-MON.

Family and domain databases

HAMAP

MF_00743.
[Tree]

InterPro

IPR003031. D_crystallin.
IPR005677. Fum_hydII.
IPR018951. Fumarase_C_C.
IPR000362. Fumarate_lyase.
[Graphical view]

Pfam

PF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]

PRINTS

PR00145. DCRYSTALLIN.
PR00149. FUMRATELYASE.

TIGRFAMs

TIGR00979. fumC_II. 1 hit.

PROSITE

PS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]

ProtoNet

Search...

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Entry information

Entry name

FUMC_ECOLI

Accession

Primary (citable) accession number: P05042
Secondary accession number(s): P76891

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	August 13, 1987
Last modified:	June 16, 2009
This is version 104 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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